Fig. 2: Characterization of the BRCA2-MEILB2-BRME1 ternary complex. | Nature Communications

Fig. 2: Characterization of the BRCA2-MEILB2-BRME1 ternary complex.

From: The BRCA2-MEILB2-BRME1 complex governs meiotic recombination and impairs the mitotic BRCA2-RAD51 function in cancer cells

Fig. 2

a Schematic of interactions between BRCA2, MEILB2, and BRME1. MBD; MEILB2-binding domain, ARM repeat; armadillo-repeat domain. b Coomassie-stained gel of the heterocomplex of MEILB2 (a.a. 87–338; 27.8 kDa) and BRCA2 (a.a. 2219–2285; 10.3 kDa). The peak fractions from the size-exclusion chromatography (right graph) are shown. Purification of the individual proteins is shown in Supplementary Fig. 2a. c SEC-MALS analysis of MEILB2 (a.a. 87–338), BRCA2 (a.a. 2219–2285), and their heterocomplex. Differential refractive index (dRI) profiles are overlaid with fitted molecular weights. d IP with the GFP antibody from B16-F1 cells expressing FLAG-BRME1 and MEILB2-MYC and GFP-BRCA2 truncations; N (a.a. 1–981), M (a.a. 982–2035), and C (a.a. 2036–3329). e Quantitative mass spectrometry of BRME1 IP (vertical axis) and control IgG IP (horizontal axis). Combined peptide intensities are plotted for each protein. Genes involved in meiotic HR regulation are indicated. Note that the other DNA repair factors, such as RAD51, were not detected by the mass spectrometry analysis, likely owing to the limited sensitivity. f, g IPs from mouse testis extracts with the BRME1 (F) or BRCA2 (G) antibodies. Asterisk: IgG heavy chain. h Protein interaction map, identified by mass spectrometry and western blotting.

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